Infrared absorption study of human hemoglobin .ALPHA.-chain (123-136) fragments in dichloromethane.
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概要
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In connection with the relationship between the conformation and solubility of peptide intermediates having polar side chains, IR spectroscopic conformational analysis of peptide fragments of human hemoglobin α-chain (123–136) was performed in dichloromethane. In dichloromethane, the conformational behavior of the peptide fragments was, in essence, dependent on their amino acid sequences, and Boc–Ser(Bzl)–Thr(Bzl)–Val–Leu–OPac through Boc–Ala–Ser(Bzl)–Val–Ser(Bzl)–Thr(Bzl)–Val–Leu–OPac had predominantly unordered structures including some intramolecular hydrogen bonds, while Boc–Ala–Ser(Bzl)–Leu–Asp(OBzl)–Lys(Z)–Phe–Leu–OPac had successive intramolecular hydrogen bonds, probably corresponding to an α-helical structure. On the other hand, in carbon tetrachloride, the conformation of Boc–Val–Ser(Bzl)–Thr(Bzl)–Val–Leu–OPac and Boc–Ser(Bzl)–Val–Ser(Bzl)–Thr(Bzl)–Val–Leu–OPac had a typical β-sheet structure. These results are discussed on the basis of the amino acid sequences of the peptide fragments.
- 公益社団法人 日本化学会の論文
著者
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Narita Mitsuaki
Department Of Biotechnology And Life Science Faculty Of Technology Tokyo University Of Agriculture A
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Doi Masamitsu
Department Of Materials Science Wakayama National College Of Technology
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Nakai Takao
Department of Industrial Chemistry, Faculty of Technology, Tokyo University of Agriculture and Technology
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Doi Masamitsu
Department of Industrial Chemistry, Faculty of Technology, Tokyo University of Agriculture and Technology
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